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Journal of Bacteriology, May 2000, p. 2869-2878, Vol. 182, No. 10
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The ssu Locus Plays a Key Role in Organosulfur Metabolism in Pseudomonas putida S-313

Antje Kahnert,1 Paul Vermeij,1,dagger Claudia Wietek,1 Peter James,2 Thomas Leisinger,1 and Michael A. Kertesz1,3,*

Institute of Microbiology1 and Protein Chemistry Laboratory,2 Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092 Zürich, Switzerland, and School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom3

Received 7 October 1999/Accepted 15 February 2000

Pseudomonas putida S-313 can utilize a broad range of aromatic sulfonates as sulfur sources for growth in sulfate-free minimal medium. The sulfonates are cleaved monooxygenolytically to yield the corresponding phenols. miniTn5 mutants of strain S-313 which were no longer able to desulfurize arylsulfonates were isolated and were found to carry transposon insertions in the ssuEADCBF operon, which contained genes for an ATP-binding cassette-type transporter (ssuABC), a two-component reduced flavin mononucleotide-dependent monooxygenase (ssuED) closely related to the Escherichia coli alkanesulfonatase, and a protein related to clostridial molybdopterin-binding proteins (ssuF). These mutants were also deficient in growth with a variety of other organosulfur sources, including aromatic and aliphatic sulfate esters, methionine, and aliphatic sulfonates other than the natural sulfonates taurine and cysteate. This pleiotropic phenotype was complemented by the ssu operon, confirming its key role in organosulfur metabolism in this species. Further complementation analysis revealed that the ssuF gene product was required for growth with all of the tested substrates except methionine and that the oxygenase encoded by ssuD was required for growth with sulfonates or methionine. The flavin reductase SsuE was not required for growth with aliphatic sulfonates or methionine but was needed for growth with arylsulfonates, suggesting that an alternative isozyme exists for the former compounds that is not active in transformation of the latter substrates. Aryl sulfate ester utilization was catalyzed by an arylsulfotransferase, and not by an arylsulfatase as in the related species Pseudomonas aeruginosa.

* Corresponding author. Mailing address: School of Biological Sciences, University of Manchester, Stopford Bldg., Oxford Rd., Manchester M13 9PT, England. Phone: 44-161-275 3895. Fax: 44-161-275 5656. E-mail: michael.kertesz{at}man.ac.uk.

dagger Present address: Intervet International B.V., NL-5830 AA Boxmeer, The Netherlands.

Journal of Bacteriology, May 2000, p. 2869-2878, Vol. 182, No. 10
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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